Myosin filamentogenesis: Effects of pH and ionic concentration

Kaminer, Benjamin; Bell, Allen L.

doi:10.1016/0022-2836(66)90070-2

Cited by 147 publications

(65 citation statements)

References 11 publications

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“…This is unlike the behavior of purified skeletal muscle myosins in vitro where filaments have a relatively large length distribution (63,64). In the case of skeletal muscle myosin, the formation of filaments has been divided into two stages, an initial stage where an antiparallel array of molecules is formed and acts as a nucleus upon which further molecules are added, via parallel interactions, to form relatively large filaments, often many microns in length (65).…”

Section: Paralogmentioning

confidence: 90%

Characterization of Three Full-length Human Nonmuscle Myosin II Paralogs

Billington

Wang

Mao

et al. 2013

Journal of Biological Chemistry

182

286

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Background: Three genes encode human nonmuscle myosin II (NM II) heavy chains, and the proteins have different intracellular roles and localizations. Results: NM II paralogs form bipolar filaments, but there are important differences in filament structure, enzymatic, and actin binding behavior. Conclusion: NM II filaments show diverse interactions with actin. Significance: NM II filaments are adapted to work in cytoskeletal networks.

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Section: Paralogmentioning

confidence: 90%

Characterization of Three Full-length Human Nonmuscle Myosin II Paralogs

Billington

Wang

Mao

et al. 2013

Journal of Biological Chemistry

182

286

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“…However, no apparent difference was noted in negatively stained preparations after the addition of low concentrations of ATP (16). Subsequently, Kaminer and Bell characterized synthetic myosin aggregates formed by varying the ionic strength and pH of the myosin solutions during filament formation (20). Filaments formed at an ionic strength of 0.1 M KCI had different structures depending on the pH.…”

Section: Structure Of Synthetic Myosin Filamentsmentioning

confidence: 99%

Quantitative studies on the polarization optical properties of striated muscle. I. Birefringence changes of rabbit psoas muscle in the transition from rigor to relaxed state.

Dl¹

1976

The Journal of Cell Biology

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The changes in birefringence in the rigor to relax transition of single tritonextracted rabbit psoas muscle fibers have been investigated with quantitative polarized light techniques. The total birefringence of rest length fibers in rigor was (1.46 -4-0.08) x 10 -s and increased to (1.67 • 0.05) • 10 -s after Mg-ATP relaxation. Pyrophosphate relaxation increased the total birefringence only slightly, whereas subsequent Mg-ATP relaxation elicited the maximum increase in birefringence. Changes in lattice spacing did not account for the total increase in birefringence during relaxation. Moreover, the increase in total birefringence was attributable to increases in intrinsic birefringence as well as form birefringence. No change in birefringence was exhibited upon exposure to a relaxation solution after myosin extraction.Synthetic myosin filaments were prepared and treated with relaxation and rigor solutions. The negatively stained filaments treated with a rigor solution had gross irregular projections at either end, while the filaments treated with a relaxing solution were more spindle shaped. The results are compatible with the view that the subfragment-2 moieties of myosin angle away from the myosin aggregates (light meromyosin) to permit the attachment of the subfragment-I moieties to actin.It is commonly accepted that the force generation mechanism in vertebrate striated muscle involves the angular movements of the subfragment-I (S-I) moieties upon attachment to the actin filaments (16,15,9,27). However, a simple mechanical interaction between the S-I moieties and actin is not possible since the center-to-center spacing between actin and myosin varies at different sarcomere lengths (18). At rest length (ca. 2.70 /~m) in rabbit psoas muscle, the surface-to-surface spacing between actin and myosin is greater than the largest lengths attributed to the S-I moieties of myosin (16,23,25).H. E. Huxley postulated that the subfragment-2 (S-2) moieties of myosin might function as hinges between the light meromyosin (LMM) backbones and the S-I moieties of myosin. Therefore the movements of S-2 moieties away from the long axis of the myosin backbones would permit the attachment of the S-I moieties at the same orienta-

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“…A different morphological class of synthetic thick filaments formed at pH 7.0 at 5 ~ C has frequently been used in studies on the role of C-protein in thick filament assembly. These filaments can have mean lengths dose to the precise length of native filaments but are otherwise dissimilar in that they are thicker and generally lack a discernable bare zone at their centres (Josephs & Harrington, 1+966;Kaminer & Bell, 1966) It has been suggested that these structural features arise from the binding of adventitous myosin to the surface of pH 8.0 type filaments (Kaminer & Bell, 1966). Under these solvent conditions the filaments carry a greater number of positively charged groups than they do under physiological conditions.…”

Section: Introductionmentioning

confidence: 97%

“…Filament form is closely linked to protein charge. Changes in pH, and to a lesser extent ionic strength and temperature, alter their structure (Josephs & Harrington, 1966;Kaminer & Bell, 1966;Davis, 1985Davis, , 1986. The pH 8.0 synthetic thick filaments ( a class of filaments formed between pH 8.0 and 8.5 at 5~ mentioned earlier were selectedl Characteristically, they appear as a homogeneous population of polymers shorter in length than native filaments with a narrow length distribution (0.65 + 0.07 ~m SD, n = 125 (Davis, 1985)) and a filament backbone diameter of 12.5 nm (Josephs & Harrington, 1966).…”

Section: Introductionmentioning

confidence: 99%

Interaction of C-protein with pH 8.0 synthetic thick filaments prepared from the myosin of vertebrate skeletal muscle

Davis

1988

J Muscle Res Cell Motil

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The assembly mechanism of synthetic thick filaments of purified myosin formed at pH 8.0 has been extensively studied. These filaments were chosen for experimentation since they share a number of structural features, as well as aspects of the kinetics of their assembly, with native filaments. C-protein copolymerization consistently favours the formation of longer synthetic filaments with the diameter of the crossbridge region remaining comparable to that of the native filament. At moderate concentrations the close-to-symmetrical length distribution typical of pH 8.0 filaments is altered to a distribution with a steep rising, and extended tailing edge towards longer filament lengths. The asymmetric length distributions probably originate from an at least partial exclusion of C-protein from the equivalent of the accessory-protein binding stripes adjacent to the bare zone from which C-protein is apparently excluded in vivo. An outer limit to C-protein binding exists in native filaments. This does not appear to be the case in vitro since filaments significantly longer than the native appear stabilized by C-protein. A minimum of three types of C-protein binding can be resolved. Physiological stoichiometries of C-protein (0 to approximately 0.3 mole ratios) lower the critical concentration of myosin (not length equilibrated) and increase filament length. The lack of a significant change in filament turbidity as these high-affinity sites are occupied is indicative of a C-protein-induced change in the structure of the synthetic filaments. A second set of binding sites occupied at higher mole ratios of C-protein: myosin (approximately 0.3-1.0) are typified by a marked increase in the specific turbidity of the filaments; a result consistent with the addition of weight to such a structure. The precedent of C-protein binding to the subfragment-2 portion of the myosin molecule provides a plausible basis for these observations. A third phase characterized by a less marked increase in turbidity occurs between 1-2:1 (and possibly higher) C-protein: myosin mole ratios. The molecular basis of this process is not immediately apparent.

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Myosin filamentogenesis: Effects of pH and ionic concentration

Cited by 147 publications

References 11 publications

Characterization of Three Full-length Human Nonmuscle Myosin II Paralogs

Characterization of Three Full-length Human Nonmuscle Myosin II Paralogs

Quantitative studies on the polarization optical properties of striated muscle. I. Birefringence changes of rabbit psoas muscle in the transition from rigor to relaxed state.

Interaction of C-protein with pH 8.0 synthetic thick filaments prepared from the myosin of vertebrate skeletal muscle

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